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Three-dimensional structure of a thermophilic family GH11 xylanase from Thermobifida fusca

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JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
DatePublished - Feb 2012
Issue number2
Volume68
Number of pages4
Pages (from-to)141-144
Original languageEnglish

Abstract

Thermostable enzymes employ various structural features dictated at the amino-acid sequence level that allow them to maintain their integrity at higher temperatures. Many hypotheses as to the nature of thermal stability have been proposed, including optimized core hydrophobicity and an increase in charged surface residues to enhance polar solvent interactions for solubility. Here, the three-dimensional structure of the family GH11 xylanase from the moderate thermophile Thermobifida fusca in its trapped covalent glycosyl-enzyme intermediate complex is presented. Interactions with the bound ligand show fewer direct hydrogen bonds from ligand to protein than observed in previous complexes from other species and imply that binding of the xylan substrate involves several water-mediated hydrogen bonds.

    Research areas

  • GLYCOSYL-ENZYME INTERMEDIATE, DIRECTED EVOLUTION, CRYSTALLOGRAPHY, xylanases, THERMAL-STABILITY, MOLECULAR-GRAPHICS, HYDROLYSIS, CONFORMATION, PROTEINS, covalent intermediate, thermostability, glycoside hydrolases, BETA-1,4-XYLANASES, COMPLEXES

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